About: Variable Oligomerization Modes in Coronavirus Non-structural Protein 9

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Variable Oligomerization Modes in Coronavirus Non-structural Protein 9
Creator	Hilgenfeld, Rolf Ponnusamy, Rajesh Moll, Ralf Mesters, Jeroen Weimar, Thomas
Source	Elsevier; Medline; PMC
abstract	Abstract Non-structural protein 9 (Nsp9) of coronaviruses is believed to bind single-stranded RNA in the viral replication complex. The crystal structure of Nsp9 of human coronavirus (HCoV) 229E reveals a novel disulfide-linked homodimer, which is very different from the previously reported Nsp9 dimer of SARS coronavirus. In contrast, the structure of the Cys69Ala mutant of HCoV-229E Nsp9 shows the same dimer organization as the SARS-CoV protein. In the crystal, the wild-type HCoV-229E protein forms a trimer of dimers, whereas the mutant and SARS-CoV Nsp9 are organized in rod-like polymers. Chemical cross-linking suggests similar modes of aggregation in solution. In zone-interference gel electrophoresis assays and surface plasmon resonance experiments, the HCoV-229E wild-type protein is found to bind oligonucleotides with relatively high affinity, whereas binding by the Cys69Ala and Cys69Ser mutants is observed only for the longest oligonucleotides. The corresponding mutations in SARS-CoV Nsp9 do not hamper nucleic acid binding. From the crystal structures, a model for single-stranded RNA binding by Nsp9 is deduced. We propose that both forms of the Nsp9 dimer are biologically relevant; the occurrence of the disulfide-bonded form may be correlated with oxidative stress induced in the host cell by the viral infection.
has issue date	2008-11-28(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2008.07.071
bibo:pmid	18694760
has license	els-covid
sha1sum (hex)	ef9ef4544974adca08fac249d0a1102cadf2ff0e
schema:url	https://doi.org/10.1016/j.jmb.2008.07.071
resource representing a document's title	Variable Oligomerization Modes in Coronavirus Non-structural Protein 9
has PubMed Central identifier	PMC7094590
has PubMed identifier	18694760
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:ef9ef4544974adca08fac249d0a1102cadf2ff0e#body_text
is schema:about of	named entity 'VARIABLE' named entity 'NON-' named entity 'protein' named entity 'RNA' named entity 'SOLUTION' named entity 'POLYMERS' named entity 'PREVIOUSLY' named entity 'EXPERIMENTS' named entity 'MODEL' named entity 'DO NOT' named entity 'OCCURRENCE' named entity 'NON-' named entity 'CHEMICAL' named entity 'REVEALS' named entity 'SARS CORONAVIRUS' named entity 'HAMPER' named entity 'DIMERS' named entity 'CRYSTAL STRUCTURE' named entity 'RNA' named entity 'OXIDATIVE STRESS' named entity 'LONGEST' named entity 'ORGANIZATION' named entity '229E' named entity 'CORRELATED' named entity 'MAY BE' named entity 'DISULFIDE' named entity 'SINGLE-STRANDED RNA BINDING' named entity 'NOVEL' named entity 'HIGH' named entity 'CRYSTAL' named entity 'SURFACE PLASMON RESONANCE' named entity 'STRUCTURAL PROTEIN' named entity 'OLIGOMERIZATION' named entity 'FORMS' named entity 'AGGREGATION' named entity 'INTERFERENCE' named entity 'WILD-TYPE' named entity 'MUTANT' named entity 'STRUCTURES' named entity 'OLIGONUCLEOTIDES' named entity 'GEL ELECTROPHORESIS' named entity 'FOUND' named entity 'PROTEIN ' named entity 'ROD-LIKE' named entity 'SIMILAR' named entity 'CROSS-LINKING' named entity 'BONDED' named entity 'VIRAL INFECTION' named entity 'REPORTED' named entity 'HCOV-229E' named entity 'PROTEIN ' named entity 'CORONAVIRUS' named entity 'SARS-COV PROTEIN' named entity 'TRIMER' named entity 'ZONE' named entity 'RELEVANT' named entity 'INDUCED' named entity 'HOMODIMER' named entity 'BIND' named entity 'STRUCTURE' named entity 'FORM' named entity 'CONTRAST' named entity 'ORGANIZED' named entity 'HUMAN CORONAVIRUS' named entity 'SARS-COV' named entity 'BINDING' named entity 'STRUCTURAL PROTEIN' named entity 'OBSERVED' named entity 'HOST CELL' named entity 'MUTATIONS' named entity 'NUCLEIC ACID BINDING' named entity 'AFFINITY' named entity 'BIOLOGICALLY' named entity 'DIMER' named entity 'CORONAVIRUSES' named entity 'VIRAL REPLICATION COMPLEX' named entity 'DIFFERENT'

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